Zobrazeno 1 - 10 of 442 pro vyhledávání: '"TANCREDI, T."'
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Akademický článek
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The α-to-β Conformational Transition of Alzheimer's Aβ-(1-42) Peptide in Aqueous Media is Reversible: A Step by Step Conformational Analysis Suggests the Location of β Conformation Seeding
Autor: Tomaselli, S., Esposito, V., Vangone, P., van Nuland, N.A.J., Bonvin, A.M.J.J., Guerrini, R., Tancredi, T., Temussi, P.A., Picone, D., NMR-spectroscopie, Dep Scheikunde
Publikováno v: ChemBioChem
7 (2006): 257–267. doi:10.1002/cbic.200500223
info:cnr-pdr/source/autori:Tomaselli S; Esposito V; Vangone P; van Nuland NAJ; Bonvin AMJJ; Guerrini R; Tancredi T; Temussi PA; Picone D/titolo:The alpha-to-beta conformational transition of Alzheimer's A beta-(1-42) peptide in aqueous media is reversible: A step by step conformational analysis suggests the location of beta conformation seeding/doi:10.1002%2Fcbic.200500223/rivista:ChemBioChem (Print)/anno:2006/pagina_da:257/pagina_a:267/intervallo_pagine:257–267/volume:7
ChemBioChem, 7, 257. Wiley-VCH Verlag
Current views of the role of beta-amyloid (Abeta) peptide fibrils range from regarding them as the cause of Alzheimer's pathology to having a protective function. In the last few years, it has also been suggested that soluble oligomers might be the m
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4b4ada78d23969da5899038d19b29c1
https://doi.org/10.1002/cbic.200500223
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3
Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin
Autor: SPADACCINI R., CRESCENZI O., TANCREDI T., DE CASAMASSIMI N., SAVIANO G., SCOGNAMIGLIO R., DI DONATO, ALBERTO, TEMUSSI, PIERO ANDREA
Publikováno v: Journal of Molecular Biology 305 (2001): 505–514.
info:cnr-pdr/source/autori:R. Spadaccini, O. Crescenzi, T. Tancredi, N. De Casamassimi, G. Saviano, R. Scognamiglio, A. Di Donato and P.A. Temussi/titolo:Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin/doi:/rivista:Journal of Molecular Biology/anno:2001/pagina_da:505/pagina_a:514/intervallo_pagine:505–514/volume:305
The sweet protein MNEI is a construct of 96 amino acid residues engineered by linking, with a Gly-Phe dipeptide, chains B and A of monellin, a sweet protein isolated from Discoreophyllum cuminsii. Here, the solution structure of MNEI was determined o
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::be3153c5b3b6329cc917987be8e6f8ad
http://hdl.handle.net/11588/136595
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Structural determinants of protein traslocation in bacteria: conformational flexibility of SecA IRA1 loop region
Autor: Palladino, P, Saviano, Gabriella, Tancredi, T, Benedetti, E, Rossi, F, Ragone, R.
Bacteria employ the SecA motor protein to push unfolded proteins across the cytoplasmic membrane through the SecY protein-conducting channel complex. The crystal structure of the SecA–SecY complex shows that the intramolecular regulator of ATPase1
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::6e903a9a09653bb69c805fcde64bbe49
http://hdl.handle.net/11695/7485
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Structural characterization of a neurotoxic threonine-rich peptidi corresponding to the human prion protein alpha-2 helical 180-195 segment, and comparison with full length alpha-2 helix-derived peptides
Autor: Ronga L., Palladino P., Saviano G., Tancredi T., Benedetti E., Ragone R., ROSSI, FILOMENA
The 173-195 segment corresponding to the helix 2 of the globular prion protein domain is a good candidate to be one of several “spots” of intrinsic structural flexibility, which might induce local destabilization and concur to protein transformat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3730::0ec7d2cda4d69ca5b5aa8acd87168b79
http://hdl.handle.net/11588/307978
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7
Environmental constraints in the study of flexible segments of proteins
Autor: D'URSI A, ALBRIZIO S, TANCREDI T, TEMUSSI, PIERO ANDREA
The structural problem posed by ill-defined segments in protein structures is similar to those encountered in the study of most peptide hormones, with terminal tracts resembling linear peptides and loops resembling cyclic peptides. The conformational
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::a677edef1e619ef51b50697ad2d1a1c1
http://hdl.handle.net/11588/147171
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9
Structural features of the interaction between SDF-1 Analogue and the CXCR4 receptor
Autor: Palladino P., De Capua A., Pedone C., Ragone R., Saviano G., Tancredi T., Limatola C., Ragozzino D., Benedetti E., ROSSI, FILOMENA
We determined by fluorescence spectroscopy the dissociation constant, kd, of the bimolecular interaction between receptor-and ligand-derived synthetic peptides, which supports a simplified model for the interaction of chemokine SDF-1 and the CXCR-4 r
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3730::4630d769096ba94547cffc7c7ca8256c
http://hdl.handle.net/11588/488369
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